MAX Protein, Human (sf9, His-GST)

MAX protein is a transcriptional regulator that forms a complex with MYC to promote activation, or a complex with MAD to cause inhibition, binding to the core sequence 5'-CAC[GA]TG-3'. MAX acts as a repressor protein that recruits chromatin remodeling complexes with H3 "Lys-9" histone methyltransferase activity. MAX Protein, Human (sf9, His-GST) is the recombinant human-derived MAX protein, expressed by Sf9 insect cells , with N-His, N-GST labeled tag. The total length of MAX Protein, Human (sf9, His-GST) is 160 a.a., with molecular weight of ~73 kDa.

MAX, a transcription regulator, forms a sequence-specific DNA-binding protein complex either with MYC, promoting transcriptional activation, or with MAD, leading to transcriptional repression, recognizing the core sequence 5'-CAC[GA]TG-3'. MAX may act as a transcriptional repressor by recruiting a chromatin remodeling complex with H3 'Lys-9' histone methyltransferase activity and repressing MYC transcriptional activity from E-box elements. Efficient DNA binding requires dimerization with another bHLH protein. It binds DNA as a heterodimer with either MYC or MAD. MAX is part of the E2F6.com-1 complex during the G0 phase, along with various other components. It is also a component of some MLL1/MLL complexes, contributing to the regulation of gene expression. MAX interacts with SPAG9, and when in a heterodimer with MYC, it interacts with ABI1, potentially enhancing MYC:MAX transcriptional activity. MAX's versatility in forming complexes with different partners underscores its role as a key modulator of gene expression.

Human

Sf9 insect cells

N-His;N-GST

P61244 (M1-S160)

4149  [NCBI]

Approximately 73 kDa

Greater than 85% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.